(data stored in ACNUC27125 zone)

HOGENOM: PRMAR1_1_PE1606

ID   PRMAR1_1_PE1606                      STANDARD;      PRT;   82 AA.
AC   PRMAR1_1_PE1606; P26641; Q6PJ62; Q6PK31; Q96CU2; Q9P196;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Elongation factor 1-gamma; Short=EF-1-gamma;AltName:
DE   Full=eEF-1B gamma; (PRMAR1_1.PE1606).
GN   Name=EEF1G; Synonyms=EF1G; ORFNames=PRO1608;
OS   PROCHLOROCOCCUS MARINUS SUBSP. MARINUS STR. CCMP1375.
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PRMAR1_1.PE1606.
CC       Prochlorococcus marinus subsp. marinus str. CCMP1375, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:EF1G_HUMAN
CC   -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC       cellular components.
CC   -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta,
CC       and gamma.
CC   -!- INTERACTION:
CC       P24534:EEF1B2; NbExp=3; IntAct=EBI-351467, EBI-354334;
CC       P29692:EEF1D; NbExp=3; IntAct=EBI-351467, EBI-358607;
CC   -!- TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue
CC       and to a lesser extent in normal kidney, intestine, pancreas,
CC       stomach, lung, brain, spleen and liver.
CC   -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC       infection.
CC   -!- SIMILARITY: Contains 1 EF-1-gamma C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P26641; Q6PJ62; Q6PK31; Q96CU2; Q9P196; -.
DR   EMBL; X63526; CAA45089.1; -; mRNA.
DR   EMBL; Z11531; CAA77630.1; -; mRNA.
DR   EMBL; BC000384; AAH00384.1; -; mRNA.
DR   EMBL; BC006509; AAH06509.1; -; mRNA.
DR   EMBL; BC006520; AAH06520.1; -; mRNA.
DR   EMBL; BC007949; AAH07949.2; -; mRNA.
DR   EMBL; BC009865; AAH09865.1; -; mRNA.
DR   EMBL; BC013918; AAH13918.1; -; mRNA.
DR   EMBL; BC015813; AAH15813.1; -; mRNA.
DR   EMBL; BC021974; AAH21974.2; -; mRNA.
DR   EMBL; BC028179; AAH28179.1; -; mRNA.
DR   EMBL; BC031012; AAH31012.1; -; mRNA.
DR   EMBL; BC067738; AAH67738.1; -; mRNA.
DR   EMBL; M55409; AAC18414.1; -; mRNA.
DR   EMBL; AF119850; AAF69604.1; -; mRNA.
DR   IPI; IPI00937615; -.
DR   PIR; S22655; S22655.
DR   RefSeq; NP_001395.1; NM_001404.4.
DR   UniGene; Hs.144835; -.
DR   UniGene; Hs.444467; -.
DR   PDB; 1PBU; NMR; -; A=276-437.
DR   PDBsum; 1PBU; -.
DR   ProteinModelPortal; P26641; -.
DR   SMR; P26641; 1-216, 276-437.
DR   IntAct; P26641; 89.
DR   MINT; MINT-1191315; -.
DR   STRING; P26641; -.
DR   PhosphoSite; P26641; -.
DR   OGP; P26641; -.
DR   PRIDE; P26641; -.
DR   Ensembl; ENST00000329251; ENSP00000331901; ENSG00000149016.
DR   GeneID; 1937; -.
DR   KEGG; hsa:1937; -.
DR   UCSC; uc001ntm.1; human.
DR   CTD; 1937; -.
DR   GeneCards; GC11M062328; -.
DR   H-InvDB; HIX0020040; -.
DR   HGNC; HGNC:3213; EEF1G.
DR   MIM; 130593; gene.
DR   neXtProt; NX_P26641; -.
DR   PharmGKB; PA27649; -.
DR   eggNOG; prNOG15588; -.
DR   InParanoid; P26641; -.
DR   PhylomeDB; P26641; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_71; Gene Expression.
DR   NextBio; 7847; -.
DR   ArrayExpress; P26641; -.
DR   CleanEx; HS_EEF1G; -.
DR   Genevestigator; P26641; -.
DR   GermOnline; ENSG00000186676; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR001662; Transl_elong_EF1_G_con.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Gene3D; G3DSA:3.30.70.1010; Transl_elong_EF1_G_con; 1.
DR   Pfam; PF00647; EF1G; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   SUPFAM; SSF89942; Transl_elong_EF1_G_con; 1.
DR   PROSITE; PS50040; EF1G_C; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   HOGENOMDNA; PRMAR1_1.PE1606; -.
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Elongation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
SQ   SEQUENCE   82 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDSITTAASV VAAGLAVGLG AIGPGIGQGS AAQGAVEGIA RQPEAEGKIR GTLLLSFAFM
     ESLTIYGLVV ALVLLFANPF AG
//

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